791022-37-2Relevant academic research and scientific papers
Discovery of 2-(Imidazo[1,2- b]pyridazin-2-yl)acetic Acid as a New Class of Ligands Selective for the γ-Hydroxybutyric Acid (GHB) High-Affinity Binding Sites
Krall, Jacob,Bavo, Francesco,Falk-Petersen, Christina B.,Jensen, Claus H.,Nielsen, Julie O.,Tian, Yongsong,Anglani, Valeria,Kongstad, Kenneth T.,Piilgaard, Louise,Nielsen, Birgitte,Gloriam, David E.,Kehler, Jan,Jensen, Anders A.,Harps?e, Kasper,Wellendorph, Petrine,Fr?lund, Bente
, p. 2798 - 2813 (2019/05/09)
Gabazine, a γ-aminobutyric acid type A (GABAA) receptor antagonist, has previously been reported to inhibit the binding of [3H]NCS-382, a representative ligand of the high-affinity binding site for the neuroactive substance γ-hydroxy
Competitive antagonism of insect GABA receptors by iminopyridazine derivatives of GABA
Rahman, Mohammad Mostafizur,Akiyoshi, Yuki,Furutani, Shogo,Matsuda, Kazuhiko,Furuta, Kenjiro,Ikeda, Izumi,Ozoe, Yoshihisa
, p. 5957 - 5964 (2012/10/29)
A series of 4-(6-imino-3-aryl/heteroarylpyridazin-1-yl)butanoic acids were synthesized and examined for antagonism of GABA receptors from three insect species. When tested against small brown planthopper GABA receptors, the 3,4-methylenedioxyphenyl and the 2-naphthyl analogues showed complete inhibition of GABA-induced fluorescence changes at 100 μM in assays using a membrane potential probe. Against common cutworm GABA receptors, these analogues displayed approximately 86% and complete inhibition of GABA-induced fluorescence changes at 100 μM, respectively. The 4-biphenyl and 4-phenoxyphenyl analogues showed moderate inhibition at 10 μM in these receptors, although the inhibition at 100 μM was not complete. Against American cockroach GABA receptors, the 4-biphenyl analogue exhibited the greatest inhibition (approximately 92%) of GABA-induced currents, when tested at 500 μM using a patch-clamp technique. The second most active analogue was the 2-naphthyl analogue with approximately 85% inhibition. The 3-thienyl analogue demonstrated competitive inhibition of cockroach GABA receptors. Homology modeling and ligand docking studies predicted that hydrophobic 3-substituents could interact with an accessory binding site at the orthosteric binding site.
